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Effect of ATP analogues on the actin-myosin interface

机译：ATP类似物对肌动蛋白-肌球蛋白界面的影响

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The interaction between skeletal myosin subfragment 1 (S1) and filamentous actin was examined at various intermediate states of the actomyosin ATPase cycle by chemical cross-linking experiments. Reaction of the actin-S1 complex with 1-ethyl-3-[3-(dimethylamino)propyl] carbodiimide and N-hydroxysuccinimide generated products with molecular masses of 165 and 175 kDa, in which S1 loops of residues 626-647 and 567-578 were cross-linked independently to the N-terminal segment of residues 1-12 of one actin monomer, and of 265 kDa, in which the two loops were bound to the N termini of two adjacent monomers. In strong-binding complexes, i.e., without nucleotide or with ADP, S1 was sequentially cross-linked to one and then to two actin monomers. In the weak-binding complexes, two types of crosslinking pattern were observed. First, during steady-state hydrolysis of ATP or ATP gamma S at 20 degrees C, the cross-linking reaction gave rise to a small amount of unknown 200 kDa product. Second, in the presence of AMPPNP, ADP.BeFx, ADP.AlF4-, or ADP.VO43- or with S1 internally cross-linked by N,N'-p-phenylenedimaleimide, only the 265 kDa product was obtained. The presence of 200 mM salt inhibited cross-linking reactions in both weak-and strong-binding states, while it dissociated only weak-binding complexes. These results indicate that, in the weak-binding state populated with the ADP.P-i analogues, skeletal S1 interacts predominantly and with an apparent equal affinity with the N termini of two adjacent actin monomers, while these ionic contacts are much less significant in stabilizing the rigor actin-S1 complexes. They also suggest that the electrostatic actin-S1 interface is not influenced by the type of ADP.P-i analogue bound to the active site. [References: 88]
机译：通过化学交联实验，在肌动球蛋白ATP酶循环的各种中间状态下检查了骨骼肌肌球蛋白亚片段1（S1）和丝状肌动蛋白之间的相互作用。肌动蛋白-S1配合物与1-乙基-3- [3-（二甲基氨基）丙基]碳二亚胺和N-羟基琥珀酰亚胺的反应生成分子量为165和175 kDa的产物，其中S1残基为626-647和567- 578独立地交联至一个肌动蛋白单体的残基1-12和265kDa的N-末端区段，其中两个环结合至两个相邻单体的N末端。在强结合复合物中，即在没有核苷酸或没有ADP的情况下，S1顺序地交联至一个，然后至两个肌动蛋白单体。在弱结合复合物中，观察到两种类型的交联图案。首先，在20摄氏度下ATP或ATPγS的稳态水解过程中，交联反应产生了少量未知的200 kDa产物。其次，在存在AMPPNP，ADP.BeFx，ADP.AlF4-或ADP.VO43-或S1被N，N'-对苯二甲基亚胺内部交联的情况下，仅获得265 kDa产物。 200 mM盐的存在在弱结合和强结合状态下均抑制了交联反应，而仅使弱结合复合物解离。这些结果表明，在由ADP.Pi类似物组成的弱结合状态下，骨架S1主要与两个相邻肌动蛋白单体的N末端相互作用，并且具有明显相等的亲和力，而这些离子接触在稳定ADP.Pi类似物方面却没有那么重要。严格的肌动蛋白-S1复合物。他们还表明，静电肌动蛋白-S1界面不受与活性位点结合的ADP.P-i类似物类型的影响。 [参考：88]

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